6xwv: Difference between revisions

<table><tr><td colspan='2'>[[6xwv]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6XWV FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG31258 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), cal1, CAL1, Cal1, CLD2, Dmel\CG5148, CG5148, Dmel_CG5148 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6xwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwv OCA], [http://pdbe.org/6xwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xwv RCSB], [http://www.ebi.ac.uk/pdbsum/6xwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwv ProSAT]</span></td></tr>

== Publication Abstract from PubMed ==

Centromeres are microtubule attachment sites on chromosomes defined by the enrichment of histone variant CENP-A-containing nucleosomes. To preserve centromere identity, CENP-A must be escorted to centromeres by a CENP-A-specific chaperone for deposition. Despite this essential requirement, many eukaryotes differ in the composition of players involved in centromere maintenance, highlighting the plasticity of this process. In humans, CENP-A recognition and centromere targeting are achieved by HJURP and the Mis18 complex, respectively. Using X-ray crystallography, we here show how Drosophila CAL1, an evolutionarily distinct CENP-A histone chaperone, binds both CENP-A and the centromere receptor CENP-C without the requirement for the Mis18 complex. While an N-terminal CAL1 fragment wraps around CENP-A/H4 through multiple physical contacts, a C-terminal CAL1 fragment directly binds a CENP-C cupin domain dimer. Although divergent at the primary structure level, CAL1 thus binds CENP-A/H4 using evolutionarily conserved and adaptive structural principles. The CAL1 binding site on CENP-C is strategically positioned near the cupin dimerisation interface, restricting binding to just one CAL1 molecule per CENP-C dimer. Overall, by demonstrating how CAL1 binds CENP-A/H4 and CENP-C, we provide key insights into the minimalistic principles underlying centromere maintenance.

 

== References ==

[[Category: Drome]]

[[Category: Abad, M A]]

[[Category: Byron, O]]

[[Category: Heun, P]]

[[Category: Jeyaprakash, A A]]

[[Category: Lazou, V]]

[[Category: Medina-Pritchard, B]]

[[Category: Rappsilber, J]]

[[Category: Zou, J]]

[[Category: Kinetochore]]